Enzyme@MOF - Research on biocatalysts immobilized in metal-organic framework compounds
By immobilizing enzymes on solid supports, reaction processes can be controlled more effectively and enzyme stability under storage and operating conditions can be improved. The immobilized enzymes can be reused and do not need to be separated from the product in a time-consuming and costly manner. Metal-organic frameworks (MOFs) have great potential as carriers. MOFs are highly porous nanostructures with strictly defined crystallinity and large specific surface area. They offer an enormous variety of possible pore structures and geometries as well as chemical properties of the material that can be specifically influenced. By immobilizing enzymes in MOFs, reaction processes can be controlled more effectively and enzyme stability under storage and operating conditions can be improved. Thanks to the large number of possible combinations of metal nodes and linkers, there is a huge potential for combinations of enzymes and MOFs. The aim of the project in this relatively new field of research is to gain a deeper understanding of the mechanisms of enzyme immobilization in MOFs as well as of the distribution equilibrium and kinetic processes during the biocatalytic reactions of enzyme@MOF immobilizates. In this way, the influencing factors and limiting boundary conditions for the immobilization as well as the subsequent reactions are to be clearly identified and, above all, quantified in order to make the potential of MOF-based enzyme immobilizates for industrially relevant biocatalytic reactions predictable.
Fig.1: Representation of an enzyme@MOF compound. The enzyme is immobilized in a unit of the crystal structure.